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Database: UniProt
Entry: A0A0G3H7K8_9CORY
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ID   A0A0G3H7K8_9CORY        Unreviewed;       697 AA.
AC   A0A0G3H7K8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE            EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
GN   Name=pflB {ECO:0000313|EMBL:AKK08735.1};
GN   ORFNames=CTEST_06485 {ECO:0000313|EMBL:AKK08735.1};
OS   Corynebacterium testudinoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08735.1, ECO:0000313|Proteomes:UP000035540};
RN   [1] {ECO:0000313|EMBL:AKK08735.1, ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08735.1,
RC   ECO:0000313|Proteomes:UP000035540};
RX   PubMed=26227591;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT   DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL   Genome Announc. 3:e00784-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT   recovered from necrotic lesions in the mouth of a tortoise.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00001179};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000256|ARBA:ARBA00008375}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00493}.
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DR   EMBL; CP011545; AKK08735.1; -; Genomic_DNA.
DR   RefSeq; WP_047253046.1; NZ_JAASJB010000002.1.
DR   AlphaFoldDB; A0A0G3H7K8; -.
DR   STRING; 136857.CTEST_06485; -.
DR   KEGG; cted:CTEST_06485; -.
DR   PATRIC; fig|136857.5.peg.1288; -.
DR   OrthoDB; 9803969at2; -.
DR   Proteomes; UP000035540; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 1.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:AKK08735.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000313|EMBL:AKK08735.1};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818};
KW   Pyruvate {ECO:0000313|EMBL:AKK08735.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035540};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKK08735.1}.
FT   DOMAIN          6..623
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          630..697
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   ACT_SITE        414
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        415
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
SQ   SEQUENCE   697 AA;  77267 MW;  757B807FFD688AFE CRC64;
     MTTVTAPDTQ AWEGFHEGPW QEAIDVRDFI SRNFTPYSGD AEFLSGPTEK TLRTWKHLED
     NYLSVERQRR VYDVDTSTPA DIDAFAPGFI SDDDNVIVGL QTDTPLKRAM MPYGGWRMVE
     TAIREANLEP NEDIKKIFTR YRKTHNEAVF DVYTPRIRAA RSSHIITGLP DAYGRGRIIG
     DYRRVALYGV DKLIAEKEAS KHAAGPQGFS EHWARFREEH SEQIKALKKL KTMAASYGFD
     ISGPAATAQE AVQWTYFGYL GAVKSQDGAA MSIGRLSSFF DIYFERDLAN GTITEEDAQE
     IIDSLVLKLR IVRFLRTIDY DQIFSGDPYW ATWSDAGFMA DGRPQVTKTS FRLLQTLRNL
     GPAPEPNITV FWDPQLPAGY KDFCAAISIE TSSIQYESDK QIRDRWGDDS AIACCVSPMA
     VGKQMQFFGA RVNAAKSLLY AINGGRDEVT GKQITTEGEF SPIEGDGPLD FDEVWNKYEE
     MLNWVIGTYV EALNIIHWSH DKYAYEAIEM ALHDSDIVRS MGCGIAGLSI VADSLSAIKY
     AKVTPVRDDT GLIVDFITEG DFPVYGNDDD RADDIAATIV HTVMAKIKEI PMYRDAIPTQ
     SVLTITSNVV YGKATGNFPS GHRAGTPFAP GANPENGADN HGMVASMLSV GKLDYHDALD
     GISLTNTITP SGLGRTKDEQ VSNLVGVLDA GFIMDEN
//
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